Paenibacillus curdlanolyticus B-6 xylanase Xyn10C capable of producing a doubly arabinose-substituted xylose, α-L-Araf-(1 → 2)-[α-L-Araf-(1 → 3)]-D-Xylp, from rye arabinoxylan

บทความในวารสาร

ผู้เขียน/บรรณาธิการ

กลุ่มสาขาการวิจัยเชิงกลยุทธ์

ไม่พบข้อมูลที่เกี่ยวข้อง

รายละเอียดสำหรับงานพิมพ์

รายชื่อผู้แต่ง: Imjongjairak S., Jommuengbout P., Karpilanondh P., Katsuzaki H., Sakka M., Kimura T., Pason P., Tachaapaikoon C., Romsaiyud J., Ratanakhanokchai K., Sakka K.

ผู้เผยแพร่: Elsevier

ปีที่เผยแพร่ (ค.ศ.): 2015

วารสาร: Enzyme and Microbial Technology (0141-0229)

Volume number: 72

หน้าแรก: 1

หน้าสุดท้าย: 9

จำนวนหน้า: 9

นอก: 0141-0229

eISSN: 1879-0909

URL: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84923628205&doi=10.1016%2fj.enzmictec.2015.02.002&partnerID=40&md5=70885fda4566f8dc6018c1f29dc16dcb

ภาษา: English-Great Britain (EN-GB)

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บทคัดย่อ

Paenibacillus curdlanolyticus B-6 Xyn10C is a single module xylanase consisting of a glycoside hydrolase family-10 catalytic module. The recombinant enzyme, rXyn10C, was produced by Escherichia coli and characterized. rXyn10C was highly active toward soluble xylans derived from rye, birchwood, and oat spelt, and slightly active toward insoluble wheat arabinoxylan. It hydrolyzed xylooligosaccharides larger than xylotetraose to produce xylotriose, xylobiose, and xylose. When rye arabinoxylan and oat spelt xylan were treated with the enzyme and the hydrolysis products were analyzed by thin layer chromatography (TLC), two unknown hydrolysis products, U1 and U2, were detected in the upper position of xylose on a TLC plate. Electrospray ionization mass spectrometry and enzymatic analysis using Bacillus licheniformis α- l-arabinofuranosidase Axh43A indicated that U1 was α- L-Araf-(1 → 2)-[α- L-Araf-(1 → 3)]- D-Xylp and U2 was α-L-Araf-(1 → 2)- D-Xylp, suggesting that rXyn10C had strong activity toward a xylosidic linkage before and after a doubly arabinose-substituted xylose residue and was able to accommodate an α-1,2- and α-1,3-linked arabinose-substituted xylose unit in both the -1 and +1 subsites. A molecular docking study suggested that rXyn10C could accommodate a doubly arabinose-substituted xylose residue in its catalytic site, at subsite -1. This is the first report of a xylanase capable of producing α-L-Araf-(1 → 2)-[α-L-Araf-(1 → 3)]-D-Xylp from highly arabinosylated xylan. © 2015 Elsevier Inc.

คำสำคัญ

Arabinoxylooligosaccharides, carbohydrate-binding module, Molecular docking